2db3
From Proteopedia
(Difference between revisions)
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<StructureSection load='2db3' size='340' side='right'caption='[[2db3]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='2db3' size='340' side='right'caption='[[2db3]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2db3]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[2db3]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DB3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DB3 FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2db3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2db3 OCA], [https://pdbe.org/2db3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2db3 RCSB], [https://www.ebi.ac.uk/pdbsum/2db3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2db3 ProSAT], [https://www.topsan.org/Proteins/RSGI/2db3 TOPSAN]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2db3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2db3 OCA], [https://pdbe.org/2db3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2db3 RCSB], [https://www.ebi.ac.uk/pdbsum/2db3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2db3 ProSAT], [https://www.topsan.org/Proteins/RSGI/2db3 TOPSAN]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/VASA1_DROME VASA1_DROME] Involved in translational control mechanisms operating in early stages of oogenesis. Required maternally in many stages of oogenesis, including cystocyte differentiation, oocyte differentiation, and specification of anterior-posterior polarity in the developing cysts. Essential for the formation and/or structural integrity of perinuclear nuage particles during germ cell formation. Required for gus, Fsn and aub accumulation at the posterior pole of the embryo. Required for the localization of vas to the perinuclear region of nurse cells.<ref>PMID:10678180</ref> <ref>PMID:11526087</ref> <ref>PMID:12479811</ref> <ref>PMID:14588248</ref> <ref>PMID:16630817</ref> <ref>PMID:18590813</ref> <ref>PMID:20123973</ref> <ref>PMID:3052853</ref> <ref>PMID:3140040</ref> <ref>PMID:8026330</ref> <ref>PMID:9521895</ref> | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2db3 ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2db3 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | DEAD-box RNA helicases, which regulate various processes involving RNA, have two RecA-like domains as a catalytic core to alter higher-order RNA structures. We determined the 2.2 A resolution structure of the core of the Drosophila DEAD-box protein Vasa in complex with a single-stranded RNA and an ATP analog. The ATP analog intensively interacts with both of the domains, thereby bringing them into the closed form, with many interdomain interactions of conserved residues. The bound RNA is sharply bent, avoiding a clash with a conserved alpha helix in the N-terminal domain. This "wedge" helix should disrupt base pairs by bending one of the strands when a duplex is bound. Mutational analyses indicated that the interdomain interactions couple ATP hydrolysis to RNA unwinding, probably through fine positioning of the duplex relative to the wedge helix. This mechanism, which differs from those for canonical translocating helicases, may enable the targeted modulation of intricate RNA structures. | ||
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| - | Structural basis for RNA unwinding by the DEAD-box protein Drosophila Vasa.,Sengoku T, Nureki O, Nakamura A, Kobayashi S, Yokoyama S Cell. 2006 Apr 21;125(2):287-300. PMID:16630817<ref>PMID:16630817</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 2db3" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Drosophila melanogaster]] |
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[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Kobayashi | + | [[Category: Kobayashi S]] |
| - | [[Category: Nakamura | + | [[Category: Nakamura A]] |
| - | [[Category: Nureki | + | [[Category: Nureki O]] |
| - | + | [[Category: Sengoku T]] | |
| - | [[Category: Sengoku | + | [[Category: Yokoyama S]] |
| - | [[Category: Yokoyama | + | |
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Current revision
Structural basis for RNA unwinding by the DEAD-box protein Drosophila Vasa
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